Digestibility and IgE-Binding of Glycosylated Codfish Parvalbumin
نویسندگان
چکیده
منابع مشابه
Digestibility and IgE-Binding of Glycosylated Codfish Parvalbumin
Food-processing conditions may alter the allergenicity of food proteins by different means. In this study, the effect of the glycosylation as a result of thermal treatment on the digestibility and IgE-binding of codfish parvalbumin is investigated. Native and glycosylated parvalbumins were digested with pepsin at various conditions relevant for the gastrointestinal tract. Intact proteins and pe...
متن کاملCharacterization of IgG and IgE Binding to Parvalbumin Derived from Commercially Important Fish Species
Parvalbumin is a pan-allergen in fish and frog that triggers IgE-mediated reactions in fish-allergic individuals. Previous studies demonstrated that antibodies raised against fish and frog parvalbumins displayed varying specificity for different fish species, and thus the applicability of these antibodies for potential use in immunoassays to detect fish residues were limited. We aimed to determ...
متن کاملBinding of acrylonitrile to parvalbumin.
A previous study has shown that acrylonitrile (ACN) has a long half-life in rainbow trout muscle and that [14C]ACN appears to be bound to a 10,000-Da protein in muscle. The labeled protein was purified from muscle of trout exposed to [14C]ACN, separated on 20% SDS-PAGE, and digested for amino acid analysis and sequence analysis. These studies indicated that the labeled protein was the Ca(2+)-bi...
متن کاملThe Binding Properties of Glycosylated and Non-Glycosylated Tim-3 Molecules on CD4+CD25+ T Cells
BACKGROUND T cell immunoglobulin and mucin domain containing 3 protein (Tim-3) expressed on terminally differentiated Th1 cells plays a suppressive role in Th1-mediated immune responses. Recently, it has been shown that N-glycosylation affects the binding activity of the Tim-3-Ig fusion protein to its ligand, galectin-9, but the binding properties of non-glycosylated Tim-3 on CD4(+)CD25(+) T ce...
متن کاملEngineering Parvalbumin for the Heart: Optimizing the Mg2+ Binding Properties of Rat β-Parvalbumin
Parvalbumin (PV), an EF-hand protein family member, is a delayed calcium buffer that exchanges magnesium for calcium to facilitate fast skeletal muscle relaxation. Genetic approaches that express parvalbumin in the heart also enhance relaxation and show promise of being therapeutic against various cardiac diseases where relaxation is compromised. Unfortunately, skeletal muscle PVs have very slo...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: BioMed Research International
سال: 2013
ISSN: 2314-6133,2314-6141
DOI: 10.1155/2013/756789